1. Continued studies on the nature of phosphoryl group transfer in phosphokinases, particularly phosphoglycerate kinase. 2. Delineation of the nature of the isomerization of 2-phosphoglycerate and 3-phosphoglycerate as catalyzed by phosphoglycerate mutase. 3. Substrate analogs, transition state analogs, and inactivators of phosphoglycerate mutase. 4. The sterochemistry of phosphoryl group transfer using a phosphoryl group of known chirality. BIBLIOGRAPHIC REFERENCES: P. E. Johnson, S.J. Abbott, G. A. Orr, M. Semeriva and J. R. Knowles, "On the 'phosphoryl enzyme' of phosphoglycerate kinase," Biochem. Biophys. Res. Commun. 1975, 62, 382. A.0K. Newmark and J. R. Knowles, "Acyl- and amino-transfer routes in pepsin-catalyzed reactions," J. Amer. Chem. Soc., 1975, 97, 3557.